6WKO

Structure of an influenza C virus hemagglutinin-esterase-fusion (HEF2) intermediate

Summary for 6WKO

• Entry DOI: 10.2210/pdb6wko/pdb
• Descriptor: Hemagglutinin-esterase-fusion glycoprotein, CHLORIDE ION (3 entities in total)
• Functional Keywords: viral fusion, fusion intermediate, influenza c virus, hemagglutinin-esterase-fusion, viral protein
• Biological source: Influenza C virus (strain C/Johannesburg/1/1966)
• Total number of polymer chains: 1
• Total formula weight: 10291.96

Authors

Serrao, V.H.B.,Lee, J.E. (deposition date: 2020-04-16, release date: 2021-05-19, Last modification date: 2023-10-18)

Primary citation

Serrao, V.H.B.,Cook, J.D.,Lee, J.E.
Snapshot of an influenza virus glycoprotein fusion intermediate.
Cell Rep, 35:109152-109152, 2021

PubMed Abstract: Enveloped virus entry requires the fusion of cellular and viral membranes, a process directed by their viral fusion glycoproteins. Our current knowledge of this process has been shaped by structural studies of the pre- and post-fusion conformations of these viral fusogens. These structural snapshots have revealed the start and end states necessary for fusion, but the dynamics of the intermediate conformations have remained unclear. Using the influenza C virus hemagglutinin-esterase-fusion glycoprotein as a model, we report the structural and biophysical characterization of a trapped intermediate. Crystallographic studies revealed a structural reorganization of the C terminus to create a second chain reversal region, resulting in the N and C termini being positioned in opposing directions. Intrinsic tryptophan fluorescence and bimane-induced quenching measurements suggest intermediate formation is mediated by conserved hydrophobic residues. Our study reveals a late-stage extended intermediate structural event. This work adds to our understanding of virus cell fusion.

PubMed: 34010634
DOI: 10.1016/j.celrep.2021.109152

Experimental method

X-RAY DIFFRACTION (2.401 Å)